Sequential processing of mannose-containing glycans by two α-mannosidases from Solitalea canadensis
| Autor: | Josef Voglmeir, Li Liu, Fang F Liu, Anna Kulinich, Ya M Du |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Mannosidase Glycan Mannose Solitalea canadensis medicine.disease_cause alpha-Mannosidase Biochemistry Substrate Specificity law.invention 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins law medicine Mannosidases Molecular Biology chemistry.chemical_classification 030102 biochemistry & molecular biology biology Bacteroidetes Cell Biology 030104 developmental biology Enzyme chemistry biology.protein Recombinant DNA |
| Zdroj: | Glycoconjugate Journal. 33:159-168 |
| ISSN: | 1573-4986 0282-0080 |
| DOI: | 10.1007/s10719-016-9651-9 |
| Popis: | Two putative α-mannosidase genes isolated from the rather unexplored soil bacterium Solitalea canadensis were cloned and biochemically characterised. Both recombinant enzymes were highly selective in releasing α-linked mannose but no other sugars. The α-mannosidases were designated Sca2/3Man2693 and Sca6Man4191, and showed the following biochemical properties: the temperature optimum for both enzymes was 37 °C, and their pH optima lay at 5.0 and 5.5, respectively. The activity of Sca2/3Man2693 was found to be dependent on Ca(2+) ions, whereas Cu(2+) and Zn(2+) ions almost completely inhibited both α-mannosidases. Specificity screens with various substrates revealed that Sca2/3Man2693 could release both α1-2- and α1-3-linked mannose, whereas Sca6Man4191 only released α1-6-linked mannose. The combined enzymatic action of both recombinant α-mannosidases allowed the sequential degradation of high-mannose-type N-glycans. The facile expression and purification procedures in combination with strict substrate specificities make α-mannosidases from S. canadensis promising candidates for bioanalytical applications. |
| Databáze: | OpenAIRE |
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